JP2011500587A - マイコバクテリウム・アビウム亜種パラツベルクローシスに対する免疫応答を誘発するための組成物 - Google Patents
マイコバクテリウム・アビウム亜種パラツベルクローシスに対する免疫応答を誘発するための組成物 Download PDFInfo
- Publication number
- JP2011500587A JP2011500587A JP2010529059A JP2010529059A JP2011500587A JP 2011500587 A JP2011500587 A JP 2011500587A JP 2010529059 A JP2010529059 A JP 2010529059A JP 2010529059 A JP2010529059 A JP 2010529059A JP 2011500587 A JP2011500587 A JP 2011500587A
- Authority
- JP
- Japan
- Prior art keywords
- map
- protein
- composition
- animals
- group
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Ceased
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 48
- 230000028993 immune response Effects 0.000 title claims abstract description 19
- 208000026681 Paratuberculosis Diseases 0.000 title claims abstract description 9
- 241000186367 Mycobacterium avium Species 0.000 title claims abstract description 7
- 230000001939 inductive effect Effects 0.000 title 1
- 241001465754 Metazoa Species 0.000 claims abstract description 141
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 59
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 50
- 238000000034 method Methods 0.000 claims abstract description 42
- 241000282849 Ruminantia Species 0.000 claims abstract description 11
- 210000004900 c-terminal fragment Anatomy 0.000 claims abstract description 9
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims abstract description 7
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims abstract description 7
- 230000004936 stimulating effect Effects 0.000 claims abstract description 7
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 3
- 241000283707 Capra Species 0.000 claims description 22
- 150000001413 amino acids Chemical class 0.000 claims description 17
- 239000002671 adjuvant Substances 0.000 claims description 16
- 229940035032 monophosphoryl lipid a Drugs 0.000 claims description 16
- ZLDPNFYTUDQDMJ-UHFFFAOYSA-N n-octadecyloctadecan-1-amine;hydrobromide Chemical compound Br.CCCCCCCCCCCCCCCCCCNCCCCCCCCCCCCCCCCCC ZLDPNFYTUDQDMJ-UHFFFAOYSA-N 0.000 claims description 10
- 241000283690 Bos taurus Species 0.000 claims description 9
- 210000004898 n-terminal fragment Anatomy 0.000 claims description 8
- 229920001184 polypeptide Polymers 0.000 claims description 8
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 8
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 8
- 241000124008 Mammalia Species 0.000 claims description 7
- 201000010099 disease Diseases 0.000 claims description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 6
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 5
- PSLWZOIUBRXAQW-UHFFFAOYSA-M dimethyl(dioctadecyl)azanium;bromide Chemical compound [Br-].CCCCCCCCCCCCCCCCCC[N+](C)(C)CCCCCCCCCCCCCCCCCC PSLWZOIUBRXAQW-UHFFFAOYSA-M 0.000 claims description 3
- 241000282979 Alces alces Species 0.000 claims description 2
- 241000282994 Cervidae Species 0.000 claims description 2
- 241001494479 Pecora Species 0.000 claims description 2
- 210000004899 c-terminal region Anatomy 0.000 claims description 2
- 208000015181 infectious disease Diseases 0.000 abstract description 25
- 241000894006 Bacteria Species 0.000 abstract description 6
- 230000009286 beneficial effect Effects 0.000 abstract description 4
- 239000000427 antigen Substances 0.000 description 88
- 108091007433 antigens Proteins 0.000 description 88
- 102000036639 antigens Human genes 0.000 description 88
- 238000009448 modified atmosphere packaging Methods 0.000 description 86
- 210000004027 cell Anatomy 0.000 description 57
- 102100037850 Interferon gamma Human genes 0.000 description 43
- 108010074328 Interferon-gamma Proteins 0.000 description 43
- 230000004044 response Effects 0.000 description 42
- 241000699670 Mus sp. Species 0.000 description 26
- 230000014509 gene expression Effects 0.000 description 26
- 210000001744 T-lymphocyte Anatomy 0.000 description 25
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 23
- 210000001519 tissue Anatomy 0.000 description 22
- 210000000952 spleen Anatomy 0.000 description 20
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 19
- 239000002953 phosphate buffered saline Substances 0.000 description 19
- 238000002255 vaccination Methods 0.000 description 19
- 206010018691 Granuloma Diseases 0.000 description 17
- 210000004185 liver Anatomy 0.000 description 17
- 102100034922 T-cell surface glycoprotein CD8 alpha chain Human genes 0.000 description 16
- 230000003053 immunization Effects 0.000 description 16
- 238000002649 immunization Methods 0.000 description 16
- 230000001681 protective effect Effects 0.000 description 16
- 108090000695 Cytokines Proteins 0.000 description 13
- 210000004698 lymphocyte Anatomy 0.000 description 13
- 108700026244 Open Reading Frames Proteins 0.000 description 12
- 230000005867 T cell response Effects 0.000 description 12
- 230000005875 antibody response Effects 0.000 description 12
- 238000002965 ELISA Methods 0.000 description 11
- 108091034117 Oligonucleotide Proteins 0.000 description 11
- 230000001580 bacterial effect Effects 0.000 description 11
- 210000001165 lymph node Anatomy 0.000 description 11
- 239000000523 sample Substances 0.000 description 11
- 102000019197 Superoxide Dismutase Human genes 0.000 description 10
- 108010012715 Superoxide dismutase Proteins 0.000 description 10
- 239000000872 buffer Substances 0.000 description 10
- 210000004989 spleen cell Anatomy 0.000 description 10
- 238000010186 staining Methods 0.000 description 10
- 238000005406 washing Methods 0.000 description 10
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 9
- 238000002474 experimental method Methods 0.000 description 9
- 238000000684 flow cytometry Methods 0.000 description 9
- 210000000207 lymphocyte subset Anatomy 0.000 description 9
- 230000000638 stimulation Effects 0.000 description 8
- 102000004127 Cytokines Human genes 0.000 description 7
- 241000588724 Escherichia coli Species 0.000 description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 description 7
- 238000011888 autopsy Methods 0.000 description 7
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 6
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 6
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 6
- 239000002299 complementary DNA Substances 0.000 description 6
- 239000002158 endotoxin Substances 0.000 description 6
- 230000036541 health Effects 0.000 description 6
- 108020004999 messenger RNA Proteins 0.000 description 6
- 210000000056 organ Anatomy 0.000 description 6
- 230000000069 prophylactic effect Effects 0.000 description 6
- 230000002829 reductive effect Effects 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 229960005486 vaccine Drugs 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 5
- 239000012228 culture supernatant Substances 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 230000035755 proliferation Effects 0.000 description 5
- 230000009696 proliferative response Effects 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 4
- BZTDTCNHAFUJOG-UHFFFAOYSA-N 6-carboxyfluorescein Chemical compound C12=CC=C(O)C=C2OC2=CC(O)=CC=C2C11OC(=O)C2=CC=C(C(=O)O)C=C21 BZTDTCNHAFUJOG-UHFFFAOYSA-N 0.000 description 4
- 102000017420 CD3 protein, epsilon/gamma/delta subunit Human genes 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 238000012408 PCR amplification Methods 0.000 description 4
- 238000010171 animal model Methods 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 244000052616 bacterial pathogen Species 0.000 description 4
- 238000004043 dyeing Methods 0.000 description 4
- 238000003114 enzyme-linked immunosorbent spot assay Methods 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 210000003405 ileum Anatomy 0.000 description 4
- 210000003000 inclusion body Anatomy 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 230000006698 induction Effects 0.000 description 4
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 4
- 210000002540 macrophage Anatomy 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 235000013336 milk Nutrition 0.000 description 4
- 239000008267 milk Substances 0.000 description 4
- 210000004080 milk Anatomy 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 239000013598 vector Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- WOVKYSAHUYNSMH-RRKCRQDMSA-N 5-bromodeoxyuridine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(Br)=C1 WOVKYSAHUYNSMH-RRKCRQDMSA-N 0.000 description 3
- 108020004414 DNA Proteins 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 3
- 238000011510 Elispot assay Methods 0.000 description 3
- 241000620209 Escherichia coli DH5[alpha] Species 0.000 description 3
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 3
- 101001057504 Homo sapiens Interferon-stimulated gene 20 kDa protein Proteins 0.000 description 3
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 3
- 102100026878 Interleukin-2 receptor subunit alpha Human genes 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 206010062207 Mycobacterial infection Diseases 0.000 description 3
- 108010076039 Polyproteins Proteins 0.000 description 3
- HWPGTWGCGXNKHI-RQMZFSEBSA-N [(2S,3R)-1-[[(3S)-1-hydroxy-2-oxoazepan-3-yl]amino]-2-methyl-1-oxopentan-3-yl] (2S)-6-[[(Z)-hexadec-2-enoyl]-hydroxyamino]-2-[[(4S,5R)-2-(2-hydroxyphenyl)-5-methyl-4,5-dihydro-1,3-oxazole-4-carbonyl]amino]hexanoate Chemical compound CCCCCCCCCCCCC\C=C/C(=O)N(O)CCCC[C@H](NC(=O)[C@H]1N=C(O[C@@H]1C)c1ccccc1O)C(=O)O[C@H](CC)[C@H](C)C(=O)N[C@H]1CCCCN(O)C1=O HWPGTWGCGXNKHI-RQMZFSEBSA-N 0.000 description 3
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 3
- 229960002685 biotin Drugs 0.000 description 3
- 235000020958 biotin Nutrition 0.000 description 3
- 239000011616 biotin Substances 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 210000001072 colon Anatomy 0.000 description 3
- 235000021277 colostrum Nutrition 0.000 description 3
- 210000003022 colostrum Anatomy 0.000 description 3
- 235000013365 dairy product Nutrition 0.000 description 3
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 3
- 239000003937 drug carrier Substances 0.000 description 3
- YQGOJNYOYNNSMM-UHFFFAOYSA-N eosin Chemical compound [Na+].OC(=O)C1=CC=CC=C1C1=C2C=C(Br)C(=O)C(Br)=C2OC2=C(Br)C(O)=C(Br)C=C21 YQGOJNYOYNNSMM-UHFFFAOYSA-N 0.000 description 3
- 108020001507 fusion proteins Proteins 0.000 description 3
- 102000037865 fusion proteins Human genes 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 210000000987 immune system Anatomy 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 210000001630 jejunum Anatomy 0.000 description 3
- 239000006166 lysate Substances 0.000 description 3
- 208000027531 mycobacterial infectious disease Diseases 0.000 description 3
- 230000007935 neutral effect Effects 0.000 description 3
- 230000003287 optical effect Effects 0.000 description 3
- 230000007170 pathology Effects 0.000 description 3
- 239000013641 positive control Substances 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 239000012089 stop solution Substances 0.000 description 3
- 238000010254 subcutaneous injection Methods 0.000 description 3
- 239000007929 subcutaneous injection Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 201000008827 tuberculosis Diseases 0.000 description 3
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- WOVKYSAHUYNSMH-UHFFFAOYSA-N BROMODEOXYURIDINE Natural products C1C(O)C(CO)OC1N1C(=O)NC(=O)C(Br)=C1 WOVKYSAHUYNSMH-UHFFFAOYSA-N 0.000 description 2
- 241000701083 Bovine alphaherpesvirus 1 Species 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 108010062580 Concanavalin A Proteins 0.000 description 2
- 208000011231 Crohn disease Diseases 0.000 description 2
- 108010041986 DNA Vaccines Proteins 0.000 description 2
- 229940021995 DNA vaccine Drugs 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- 101710178629 ESAT-6-like protein Proteins 0.000 description 2
- 102000002322 Egg Proteins Human genes 0.000 description 2
- 108010000912 Egg Proteins Proteins 0.000 description 2
- 102100021186 Granulysin Human genes 0.000 description 2
- 101710168479 Granulysin Proteins 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 239000006137 Luria-Bertani broth Substances 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 238000011530 RNeasy Mini Kit Methods 0.000 description 2
- 239000012980 RPMI-1640 medium Substances 0.000 description 2
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 238000000692 Student's t-test Methods 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 229950004398 broxuridine Drugs 0.000 description 2
- 210000004534 cecum Anatomy 0.000 description 2
- 238000001516 cell proliferation assay Methods 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 231100000676 disease causative agent Toxicity 0.000 description 2
- 210000001198 duodenum Anatomy 0.000 description 2
- 235000013345 egg yolk Nutrition 0.000 description 2
- 210000002969 egg yolk Anatomy 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 238000001976 enzyme digestion Methods 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 239000012091 fetal bovine serum Substances 0.000 description 2
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 2
- 238000007654 immersion Methods 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 230000003902 lesion Effects 0.000 description 2
- 229920006008 lipopolysaccharide Polymers 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 150000007523 nucleic acids Chemical group 0.000 description 2
- ZQPPMHVWECSIRJ-KTKRTIGZSA-N oleic acid group Chemical group C(CCCCCCC\C=C/CCCCCCCC)(=O)O ZQPPMHVWECSIRJ-KTKRTIGZSA-N 0.000 description 2
- 238000001543 one-way ANOVA Methods 0.000 description 2
- 239000012188 paraffin wax Substances 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 230000005180 public health Effects 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 238000003753 real-time PCR Methods 0.000 description 2
- 238000003757 reverse transcription PCR Methods 0.000 description 2
- 101150017120 sod gene Proteins 0.000 description 2
- 238000007619 statistical method Methods 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000002459 sustained effect Effects 0.000 description 2
- 238000012549 training Methods 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- OLNJKAXRBXUBTB-JYJNAYRXSA-N (2s)-2-[[(2s)-2-[[(2s)-2-acetamido-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(O)=O)CCCN=C(N)N OLNJKAXRBXUBTB-JYJNAYRXSA-N 0.000 description 1
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- WFZFMHDDZRBTFH-CZEFNJPISA-N 2-[(e)-2-(5-carbamimidoyl-1-benzofuran-2-yl)ethenyl]-1-benzofuran-5-carboximidamide;dihydrochloride Chemical compound Cl.Cl.NC(=N)C1=CC=C2OC(/C=C/C=3OC4=CC=C(C=C4C=3)C(=N)N)=CC2=C1 WFZFMHDDZRBTFH-CZEFNJPISA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- YRNWIFYIFSBPAU-UHFFFAOYSA-N 4-[4-(dimethylamino)phenyl]-n,n-dimethylaniline Chemical compound C1=CC(N(C)C)=CC=C1C1=CC=C(N(C)C)C=C1 YRNWIFYIFSBPAU-UHFFFAOYSA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 108091093088 Amplicon Proteins 0.000 description 1
- 101000834255 Bos taurus Actin, cytoplasmic 1 Proteins 0.000 description 1
- 241000282817 Bovidae Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 241001529572 Chaceon affinis Species 0.000 description 1
- 241000759568 Corixa Species 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 102000007260 Deoxyribonuclease I Human genes 0.000 description 1
- 108010008532 Deoxyribonuclease I Proteins 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 241000672609 Escherichia coli BL21 Species 0.000 description 1
- 108700039887 Essential Genes Proteins 0.000 description 1
- 229930182566 Gentamicin Natural products 0.000 description 1
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 1
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 102000013462 Interleukin-12 Human genes 0.000 description 1
- 108010065805 Interleukin-12 Proteins 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 102000000588 Interleukin-2 Human genes 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- 229930182816 L-glutamine Natural products 0.000 description 1
- 241000239218 Limulus Species 0.000 description 1
- 239000006142 Luria-Bertani Agar Substances 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 102000043129 MHC class I family Human genes 0.000 description 1
- 108091054437 MHC class I family Proteins 0.000 description 1
- 101001044384 Mus musculus Interferon gamma Proteins 0.000 description 1
- 241000186359 Mycobacterium Species 0.000 description 1
- 229930183781 Mycobactin Natural products 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 108010056995 Perforin Proteins 0.000 description 1
- 102000004503 Perforin Human genes 0.000 description 1
- KHGNFPUMBJSZSM-UHFFFAOYSA-N Perforine Natural products COC1=C2CCC(O)C(CCC(C)(C)O)(OC)C2=NC2=C1C=CO2 KHGNFPUMBJSZSM-UHFFFAOYSA-N 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 238000002123 RNA extraction Methods 0.000 description 1
- 239000013614 RNA sample Substances 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 238000011529 RT qPCR Methods 0.000 description 1
- 108010073443 Ribi adjuvant Proteins 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 108010008038 Synthetic Vaccines Proteins 0.000 description 1
- 230000024932 T cell mediated immunity Effects 0.000 description 1
- 210000000447 Th1 cell Anatomy 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 102000006943 Uracil-DNA Glycosidase Human genes 0.000 description 1
- 108010072685 Uracil-DNA Glycosidase Proteins 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000003466 anti-cipated effect Effects 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000008350 antigen-specific antibody response Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 230000001174 ascending effect Effects 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 230000007969 cellular immunity Effects 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 208000019902 chronic diarrheal disease Diseases 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 238000001085 differential centrifugation Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000011013 endotoxin removal Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 210000003608 fece Anatomy 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 230000037406 food intake Effects 0.000 description 1
- 229960002518 gentamicin Drugs 0.000 description 1
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 1
- 238000007490 hematoxylin and eosin (H&E) staining Methods 0.000 description 1
- 244000144980 herd Species 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 210000004731 jugular vein Anatomy 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 230000006651 lactation Effects 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 210000005228 liver tissue Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 235000019837 monoammonium phosphate Nutrition 0.000 description 1
- 210000005087 mononuclear cell Anatomy 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- XZGYBQIQSLSHDH-COEJQBHMSA-N mycobactin Chemical compound C1CCCN(O)C(=O)C1NC(=O)C(C)C(CC)OC(=O)C(CCCCN(O)C(=O)\C=C/CCCCCCCCCCCCCCC)NC(=O)C(N=1)COC=1C1=C(C)C=CC=C1O XZGYBQIQSLSHDH-COEJQBHMSA-N 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 239000012053 oil suspension Substances 0.000 description 1
- 210000002741 palatine tonsil Anatomy 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 229930192851 perforin Natural products 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000005004 positive regulation of lymphocyte proliferation Effects 0.000 description 1
- 238000009021 pre-vaccination Methods 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 229940124551 recombinant vaccine Drugs 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 229940031626 subunit vaccine Drugs 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 208000016261 weight loss Diseases 0.000 description 1
- 230000004580 weight loss Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/35—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Mycobacteriaceae (F)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/02—Bacterial antigens
- A61K39/04—Mycobacterium, e.g. Mycobacterium tuberculosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/12—Antidiarrhoeals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
- A61P31/06—Antibacterial agents for tuberculosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
- C07K16/1289—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Mycobacteriaceae (F)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Communicable Diseases (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Oncology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Hematology (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Urology & Nephrology (AREA)
- Biomedical Technology (AREA)
- Pulmonology (AREA)
- Biotechnology (AREA)
- Cell Biology (AREA)
- Epidemiology (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Mycology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US97982207P | 2007-10-13 | 2007-10-13 | |
| US9455208P | 2008-09-05 | 2008-09-05 | |
| PCT/US2008/079425 WO2009049097A1 (en) | 2007-10-13 | 2008-10-09 | Compositions for eliciting an immune response against mycobacterium avium subspecies paratuberculosis |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2011500587A true JP2011500587A (ja) | 2011-01-06 |
| JP2011500587A5 JP2011500587A5 (es) | 2011-11-24 |
Family
ID=40534814
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2010529059A Ceased JP2011500587A (ja) | 2007-10-13 | 2008-10-09 | マイコバクテリウム・アビウム亜種パラツベルクローシスに対する免疫応答を誘発するための組成物 |
Country Status (18)
| Country | Link |
|---|---|
| US (1) | US7732580B2 (es) |
| EP (1) | EP2200641B1 (es) |
| JP (1) | JP2011500587A (es) |
| KR (1) | KR20100098602A (es) |
| CN (1) | CN101883582B (es) |
| AU (1) | AU2008310767A1 (es) |
| BR (1) | BRPI0817892A2 (es) |
| CA (1) | CA2704178A1 (es) |
| CO (1) | CO6270338A2 (es) |
| ES (1) | ES2390996T3 (es) |
| IN (1) | IN2010DN02553A (es) |
| MX (1) | MX2010003972A (es) |
| NZ (1) | NZ584659A (es) |
| PL (1) | PL2200641T3 (es) |
| PT (1) | PT2200641E (es) |
| RU (1) | RU2489165C2 (es) |
| WO (1) | WO2009049097A1 (es) |
| ZA (1) | ZA201002553B (es) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2013151706A2 (en) | 2012-04-06 | 2013-10-10 | Cornell University | Subunit vaccine delivery platform for robust humoral and cellular immune responses |
| US9175049B2 (en) | 2012-10-24 | 2015-11-03 | The United States Of America, As Represented By The Secretary Of Agriculture | Recombinant mycobacterium avium subsp. paratuberculosis proteins induce immunity and protect against infection |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002510494A (ja) * | 1998-04-07 | 2002-04-09 | コリクサ コーポレイション | Ｍｙｃｏｂａｃｔｅｒｉｕｍｔｕｂｅｒｃｕｌｏｓｉｓ抗原の融合タンパク質およびその使用 |
| JP2004526405A (ja) * | 2000-06-20 | 2004-09-02 | コリクサ コーポレイション | Ｍｙｃｏｂａｃｔｅｒｉｕｍｔｕｂｅｒｃｕｌｏｓｉｓの融合タンパク質 |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5322858A (en) * | 1992-02-14 | 1994-06-21 | Jacobus Pharmaceutical Co. Inc. | N,N'-substituted imidodicarbonimidic diamides derived from hydroxylamines |
| US7074559B2 (en) * | 2002-03-06 | 2006-07-11 | Refents of the University of Minnesota | Mycobacterial diagnostics |
| ES2357968T3 (es) * | 2005-02-16 | 2011-05-04 | Cornell Research Foundation, Inc. | Composiciones para desencadenar una respuesta inmunitaria contra mycobacterium avium subespecie paratuberculosis. |
| US8758773B2 (en) | 2005-12-09 | 2014-06-24 | Wisconsin Alumni Research Foundation | Vaccine candidates against Johne's disease |
-
2008
- 2008-10-09 KR KR1020107010437A patent/KR20100098602A/ko not_active Application Discontinuation
- 2008-10-09 ES ES08837410T patent/ES2390996T3/es active Active
- 2008-10-09 MX MX2010003972A patent/MX2010003972A/es not_active Application Discontinuation
- 2008-10-09 WO PCT/US2008/079425 patent/WO2009049097A1/en active Application Filing
- 2008-10-09 RU RU2010119046/15A patent/RU2489165C2/ru not_active IP Right Cessation
- 2008-10-09 PL PL08837410T patent/PL2200641T3/pl unknown
- 2008-10-09 PT PT08837410T patent/PT2200641E/pt unknown
- 2008-10-09 EP EP08837410A patent/EP2200641B1/en active Active
- 2008-10-09 BR BRPI0817892 patent/BRPI0817892A2/pt not_active IP Right Cessation
- 2008-10-09 CA CA2704178A patent/CA2704178A1/en not_active Abandoned
- 2008-10-09 AU AU2008310767A patent/AU2008310767A1/en not_active Abandoned
- 2008-10-09 JP JP2010529059A patent/JP2011500587A/ja not_active Ceased
- 2008-10-09 CN CN200880119048.7A patent/CN101883582B/zh not_active Expired - Fee Related
- 2008-10-09 NZ NZ584659A patent/NZ584659A/en not_active IP Right Cessation
- 2008-10-09 US US12/248,764 patent/US7732580B2/en not_active Expired - Fee Related
-
2010
- 2010-04-12 ZA ZA2010/02553A patent/ZA201002553B/en unknown
- 2010-04-13 IN IN2553DEN2010 patent/IN2010DN02553A/en unknown
- 2010-05-13 CO CO10057537A patent/CO6270338A2/es not_active Application Discontinuation
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002510494A (ja) * | 1998-04-07 | 2002-04-09 | コリクサ コーポレイション | Ｍｙｃｏｂａｃｔｅｒｉｕｍｔｕｂｅｒｃｕｌｏｓｉｓ抗原の融合タンパク質およびその使用 |
| JP2004526405A (ja) * | 2000-06-20 | 2004-09-02 | コリクサ コーポレイション | Ｍｙｃｏｂａｃｔｅｒｉｕｍｔｕｂｅｒｃｕｌｏｓｉｓの融合タンパク質 |
Non-Patent Citations (3)
| Title |
|---|
| JPN6014013484; Ｓｋｅｉｋｙ，Ｙ．Ａ．Ｗ．，ｅｔ ａｌ．: '"Ｄｉｆｆｅｒｅｎｔｉａｌ Ｉｍｍｕｎｅ Ｒｅｓｐｏｎｓｅｓ ａｎｄ Ｐｒｏｔｅｃｔｉｖｅ Ｅｆｆｉｃａｃｙ Ｉｎｄｕｃｅｄ ｂｙ Ｃｏｍｐｏｎｅｎｔｓ ｏｆ ａ Ｔｕｂｅｒｃｕｌｏｓｉｓ Ｐｏｌｙ' Ｊ． Ｉｍｍｕｎｏｌ． Ｖｏｌ．１７２，Ｎｏ．１２, 20040615, Ｐ．７６１８-７６２８ * |
| JPN6014013486; Ｏｌｓｅｎ，Ａ．Ｗ．，ｅｔ ａｌ．: '"Ｐｒｏｔｅｃｔｉｏｎ ｏｆ Ｍｉｃｅ ｗｉｔｈ ａ Ｔｕｂｅｒｃｕｌｏｓｉｓ Ｓｕｂｕｎｉｔ Ｖａｃｃｉｎｅ Ｂａｓｅｄ ｏｎ ａ Ｆｕｓｉｏｎ Ｐｒｏｔｅｉｎ ｏｆ Ａｎｔｉｇｅｎ ８５Ｂ ａｎ' Ｉｎｆｅｃｔ． Ｉｍｍｕｎｏｌ． Ｖｏｌ．６９，Ｎｏ．５, 200105, Ｐ．２７７３-２７７８ * |
| JPN6014013488; Ｆａｎｇ，Ｃ．Ｍ．，ｅｔ ａｌ．: '"Ｃｌｏｎｉｎｇ， ｅｘｐｒｅｓｓｉｏｎ， ａｎｄ ｐｕｒｉｆｉｃａｔｉｏｎ ｏｆ ｒｅｃｏｍｂｉｎａｎｔ ｐｒｏｔｅｉｎ ｆｒｏｍ ａ ｓｉｎｇｌｅ ｓｙｎｔｈｅｔｉｃ ｍｕｌｔｉｖａｌｅｎｔ ｃ' Ｐｒｏｔｅｉｎ Ｅｘｐｒ． Ｐｕｒｉｆ． Ｖｏｌ．４７，Ｎｏ．２, 200606, Ｐ．３４１-３４７ * |
Also Published As
| Publication number | Publication date |
|---|---|
| EP2200641A4 (en) | 2010-09-29 |
| IN2010DN02553A (es) | 2015-07-24 |
| RU2010119046A (ru) | 2011-11-20 |
| NZ584659A (en) | 2011-09-30 |
| WO2009049097A1 (en) | 2009-04-16 |
| MX2010003972A (es) | 2010-08-09 |
| KR20100098602A (ko) | 2010-09-08 |
| CO6270338A2 (es) | 2011-04-20 |
| CA2704178A1 (en) | 2009-04-16 |
| PL2200641T3 (pl) | 2012-12-31 |
| ES2390996T3 (es) | 2012-11-20 |
| RU2489165C2 (ru) | 2013-08-10 |
| BRPI0817892A2 (pt) | 2015-05-05 |
| AU2008310767A1 (en) | 2009-04-16 |
| EP2200641B1 (en) | 2012-07-04 |
| US20090099083A1 (en) | 2009-04-16 |
| EP2200641A1 (en) | 2010-06-30 |
| CN101883582A (zh) | 2010-11-10 |
| CN101883582B (zh) | 2014-03-19 |
| US7732580B2 (en) | 2010-06-08 |
| ZA201002553B (en) | 2010-12-29 |
| PT2200641E (pt) | 2012-10-11 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Corbel | Brucellosis: an overview. | |
| Hermon-Taylor et al. | Causation of Crohn’s disease by Mycobacterium avium subspecies paratuberculosis | |
| Maurin et al. | Q fever | |
| Olsen et al. | Protection against Chlamydia trachomatis infection and upper genital tract pathological changes by vaccine-promoted neutralizing antibodies directed to the VD4 of the major outer membrane protein | |
| Faisal et al. | Evaluation of protective immunity of Leptospira immunoglobulin like protein A (LigA) DNA vaccine against challenge in hamsters | |
| Rosseels et al. | Vaccination against paratuberculosis | |
| Kathaperumal et al. | Evaluation of immune responses and protective efficacy in a goat model following immunization with a coctail of recombinant antigens and a polyprotein of Mycobacterium avium subsp. paratuberculosis | |
| KR20060129475A (ko) | 에를리히아증에 대한 보호용 개 백신 | |
| Faisal et al. | Evaluation of a Salmonella vectored vaccine expressing Mycobacterium avium subsp. paratuberculosis antigens against challenge in a goat model | |
| Chen et al. | Immune responses in mice to Mycobacterium avium subsp. paratuberculosis following vaccination with a novel 74F recombinant polyprotein | |
| Stabel et al. | Comparison of Sheep, Goats, and Calves as Infection Models for Mycobacterium avium subsp. paratuberculosis | |
| Park et al. | Immunization with a DNA vaccine cocktail induces a Th1 response and protects mice against Mycobacterium avium subsp. paratuberculosis challenge | |
| Kilgore et al. | Combinatorial viral vector-based and live attenuated vaccines without an adjuvant to generate broader immune responses to effectively combat pneumonic plague | |
| US7732580B2 (en) | Compositions for eliciting an immune response against Mycobacterium avium subspecies paratuberculosis | |
| JP5038911B2 (ja) | マイコバクテリウム・アヴィウム・亜種パラチュバキュローシスに対する免疫反応を誘発するための組成物 | |
| Vordermeier et al. | Development of cattle TB vaccines in the UK | |
| Mshelia et al. | Bovine venereal campylobacteriosis: an overview. | |
| Vasconcellos et al. | Vaccine Against Entheropathogenic E. coli: A Systematic Review | |
| Olsen | Vaccination of cats against emerging and reemerging zoonotic pathogens | |
| Poston | T-cell Dependent and independent mechanisms of chlamydial eradication and control | |
| Hanafy | Immunopathogenesis of Non-Tuberculous Mycobacteria | |
| Chaitanya et al. | Immune responses to an inactivated Johne’s disease vaccine in cattle | |
| Obradovic | Identification of Lawsonia intracellularis proteins recognized by neutralizing antibodies and use of these proteins to design a subunit vaccine | |
| World Health Organization | The development of new/improved brucellosis vaccines: report of a WHO meeting, Geneva, Switzerland, 11-12 December 1997 | |
| CA3176303A1 (en) | Compositions and methods for preventing, controlling and diagnosing mycobacterial infections |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20111006 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20111006 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20130319 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20130612 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20130619 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20130719 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20130726 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20130816 |
|
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20140408 |
|
| A045 | Written measure of dismissal of application [lapsed due to lack of payment] |
Free format text: JAPANESE INTERMEDIATE CODE: A045 Effective date: 20140826 |